TOB1_RAT
ID TOB1_RAT Reviewed; 365 AA.
AC Q8R5K6;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Protein Tob1;
DE AltName: Full=Transducer of erbB-2 1;
GN Name=Tob1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Tu Y., Gao X., Jing N.;
RT "Cloning and characterization of rat tob.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH CPEB3.
RX PubMed=21336257; DOI=10.1038/emboj.2011.37;
RA Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y., Miyagawa R.,
RA Ogami K., Tsujimoto M., Hoshino S.;
RT "Anti-proliferative protein Tob negatively regulates CPEB3 target by
RT recruiting Caf1 deadenylase.";
RL EMBO J. 30:1311-1323(2011).
CC -!- FUNCTION: Anti-proliferative protein; the function is mediated by
CC association with deadenylase subunits of the CCR4-NOT complex. Mediates
CC CPEB3-accelerated mRNA deadenylation by binding to CPEB3 and recruiting
CC CNOT7 which leads to target mRNA deadenylation and decay.
CC {ECO:0000250|UniProtKB:P50616}.
CC -!- SUBUNIT: Interacts with ERBB2 (By similarity). Interacts with CNOT7 (By
CC similarity). Interacts with CPEB3 (via C-terminal RNA-binding region);
CC recruits CNOT7 to CPEB3 to form a ternary complex required for mRNA
CC deadenylation and decay (PubMed:21336257). Interacts with CNOT8 (By
CC similarity). Interacts with CPEB4 (By similarity).
CC {ECO:0000250|UniProtKB:P50616, ECO:0000269|PubMed:21336257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Only a small fraction localizes to the cytoplasm except in late S-
CC phase where more than half of proteins become cytoplasmic.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser and Thr residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
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DR EMBL; AF349723; AAL79524.1; -; mRNA.
DR AlphaFoldDB; Q8R5K6; -.
DR SMR; Q8R5K6; -.
DR MINT; Q8R5K6; -.
DR STRING; 10116.ENSRNOP00000064047; -.
DR PaxDb; Q8R5K6; -.
DR RGD; 621126; Tob1.
DR eggNOG; KOG4006; Eukaryota.
DR InParanoid; Q8R5K6; -.
DR PhylomeDB; Q8R5K6; -.
DR PRO; PR:Q8R5K6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISO:RGD.
DR Gene3D; 3.90.640.90; -; 1.
DR InterPro; IPR002087; Anti_prolifrtn.
DR InterPro; IPR036054; BTG-like_sf.
DR InterPro; IPR015677; Tob1.
DR InterPro; IPR015676; Tob1/2.
DR PANTHER; PTHR17537; PTHR17537; 1.
DR PANTHER; PTHR17537:SF6; PTHR17537:SF6; 1.
DR Pfam; PF07742; BTG; 1.
DR PRINTS; PR00310; ANTIPRLFBTG1.
DR SMART; SM00099; btg1; 1.
DR SUPFAM; SSF160696; SSF160696; 1.
DR PROSITE; PS00960; BTG_1; 1.
DR PROSITE; PS01203; BTG_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..365
FT /note="Protein Tob1"
FT /id="PRO_0000143814"
FT REGION 82..92
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..220
FT /note="Required for interaction with CPEB3"
FT /evidence="ECO:0000250|UniProtKB:P50616"
FT REGION 233..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..39
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 228..236
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 243..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50616"
SQ SEQUENCE 365 AA; 40461 MW; C202986337E6C350 CRC64;
MQLEIQVALN FIISYLYNKL PRRRVNIFGE ELERLLKQKY EGHWYPEKPY KGSGFRCIHV
GEKVDPVIEQ ASKESGLDID DVRGNLPQDL SVWIDPFEVS YQIGEKGPVK VLYVDDSNEN
GCELDKEIKN SFNPEAQVFM PISDPASSVS SSPSPPFGHS AAVSPTFMPR STQPLTFTTA
TFAATKFGST KMKNSGRSSK VARTSPISLG LNVNVNDLLK QKAISSSMHS LYGLGLGSQQ
QPQPQPQQPP SQPPPPPPPP QQQQQHQQQQ QQQQQQQQQP QQQTSALSPN AKEFIFPNMQ
GQGSSTNGMF PGDSPLNLSP LQYSNAFNVF AAYGGLNEKS FVDGLNFSLN NIQYSNQQFQ
PVMAN
